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Chenguang Cai

Publications -  10
Citations -  97

Chenguang Cai is an academic researcher. The author has contributed to research in topics: Anthrax toxin & Bacillus anthracis. The author has an hindex of 6, co-authored 9 publications receiving 92 citations.

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The Structure of Tumor Endothelial Marker 8 (TEM8) Extracellular Domain and Implications for Its Receptor Function for Recognizing Anthrax Toxin

TL;DR: The TEM8 crystal structure may provide new insights into how to design PA mutants that preferentially target tumor cells, and an isolated extracellular vWA domain of the L56A T EM8 variant may serve as a potent antitoxin and a potential therapeutic treatment for anthrax infection.
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Tumor endothelium marker-8 based decoys exhibit superiority over capillary morphogenesis protein-2 based decoys as anthrax toxin inhibitors.

TL;DR: L56A, a PA-binding-affinity-elevated mutant of sTEM8, could inhibit anthrax intoxication as effectively as sCMG2 in Fisher 344 rats and pharmacokinetics showed that L56A and sT EM8 exhibit advantages over sC MG2 with better lung-targeting and longer plasma retention time, which may contribute to their enhanced protective ability in vivo.
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Deletion modification enhances anthrax specific immunity and protective efficacy of a hepatitis B core particle-based anthrax epitope vaccine.

TL;DR: This research successfully inserted the 2β2-2β3 loop of PA into the major immunodominant region (MIR) of hepatitis B virus core (HBc) protein, and removed amino acids 79-81 from the HBc MIR of theHBcL2, leading to the full protection of the immunized mice against a lethal dose anthrax toxin challenge.
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The inhibition of the interaction between the anthrax toxin and its cellular receptor by an anti-receptor monoclonal antibody

TL;DR: It is demonstrated that one of the MAbs, 4B5, could inhibit PA-CMG2 binding and could also protect the sensitive cells against an anthrax lethal toxin challenge and interfere with the intoxication of anthrax toxin.
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Secretory expression and efficient purification of recombinant anthrax toxin lethal factor with full biological activity in E. coli.

TL;DR: This work modified their previous method by codon optimization and chromatograph workflow refinement and developed an improved strategy for efficient production of rLF from the periplasm of E. coli with a purity above 95% and with a considerable yield of 5 mg/L.